Biocatalysis and Biotransformation · 2008 · 39 citations · 20 references
Life SciencesBiochemistryEnzymologyPolymer ChemistryPolymer EngineeringEnzyme CharacterizationEnzyme InhibitionEnzyme KineticsEnzyme StabilizationEnzyme-substrate RecognitionTextile FinishingActive SitesBondingCarboxyl FunctionalizationEnzymatic Cross-linkingEnzyme WashingMild Reaction ConditionsProtease Active Sites
The protease Esperase® was modified by covalent bonding with two grades of a reversible soluble-insoluble co-polymer of methacrylic acid and methyl-methacrylate, namely Eudragit® L 100 and Eudragit® S 100. The optimum reaction conditions and washing protocol were investigated and it was found that Esperase® modified with Eudragit® L 100 showed greater activity than if modified with Eudragit® S 100. This should be expected as there is a greater quantity of active sites, namely carboxyl groups, per mass of Eudragit® L 100 in comparison with Eudragit® S 100 to interact with the enzyme. Gel filtration confirmed that Eudragit® L 100 covalently bonded to Esperase®. Treatment of the modified Esperase® on wool showed that the enzyme modified with Eudragit® L 100 had greater activity towards the wool and appeared more effective in shrink resistant finishing.
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Treatment of wool fibres with subtilisin and subtilisin-PEG
Carla Silva, M. Prabaharan, Georg Gübitz et al. · Enzyme and Microbial Technology · 2005 · 90 citations · Full text